Curated Information
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Curated Information Page
PubMed Id: 16024771 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Tcherkezian J, et al. (2005) Extracellular signal-regulated kinase 1 interacts with and phosphorylates CdGAP at an important regulatory site. Mol Cell Biol 25, 6314-29 16024771
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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T769-p - CdGAP (mouse)
Orthologous residues
CdGAP (human): P782‑p, CdGAP (mouse): T769‑p, CdGAP (rat): P772‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)

T776-p - CdGAP (mouse)
Orthologous residues
CdGAP (human): T789‑p, CdGAP (mouse): T776‑p, CdGAP (rat): T779‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme, modification site within consensus motif
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  T776A mutant proteins have increased GAP activity toward Rac1 in response to RasV12 signaling.


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